Phosphorylation of the major heat shock protein of Dictyostelium discoideum.
The major heat shock protein, hsp 70, of Dictyostelium discoideum was found to be rapidly phosphorylated. Analysis of [35S]methionine- and 32Pi-labeled hsp 70 revealed that two similar but distinct proteins of about 70,000 daltons each are synthesized at a high rate after a heat shock, and that each has a phosphorylated member. The phosphorylation chiefly modifies threonine residues. Rapid turnover of the phosphate group occurs, resulting in a steady-state condition in which only about half of the hsp 70 is phosphorylated at a given time.
D003513:Cycloheximide / Q000494:pharmacology; D004023:Dictyostelium / Q000378:metabolism*; D006360:Heat-Shock Proteins; D007700:Kinetics; D008970:Molecular Weight; D010446:Peptide Fragments; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism
D006360:Heat-Shock Proteins; D010446:Peptide Fragments; D010710:Phosphates; D011506:Proteins; D013912:Threonine; D003513:Cycloheximide